Isolation of paenibacillus illinoisensis that produces cyclodextrin glucanotransferase resistant to organic solvents

Bioscience, Biotechnology and Biochemistry

Volumn 67, Issue 2, 2003, Pages 334-340

  Doukyu, Noriyuki ^a   Kuwahara, Hirokazu ^a   Aono, Rikizo ^a  

^a TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

Cyclodextrin; Cyclodextrin glucanotransferase; Organic solvent; Organic solvent tolerant; Paenibacillus illinoisensis

Indexed keywords

BACTERIA (MICROORGANISMS); PAENIBACILLUS; PAENIBACILLUS ILLINOISENSIS;

CYCLODEXTRIN; CYCLOMALTODEXTRIN GLUCANOTRANSFERASE; GLUCOSYLTRANSFERASE; ORGANIC COMPOUND; SOLVENT;

ARTICLE; BACILLUS; BIOSYNTHESIS; CHEMISTRY; CLASSIFICATION; ENZYME STABILITY; ENZYMOLOGY; ISOLATION AND PURIFICATION; METABOLISM; PH; TEMPERATURE;

BACILLUS; CYCLODEXTRINS; ENZYME STABILITY; GLUCOSYLTRANSFERASES; HYDROGEN-ION CONCENTRATION; ORGANIC CHEMICALS; SOLVENTS; TEMPERATURE;

EID: 0042628136     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.67.334     Document Type: Article

References (17)

1. Szejtli, J., The cyclodextrins and their applications in biotechnology. Carbohydr. Polym., 12, 375-392 (1992).
2. Mori, S., Goto, M., Mase, T., Matsuura, A., Oya, T., and Kitahata, S., Reaction conditions for the production of g-cyclodextrin glucanotransferase from Brevibacterium sp. No. 9605. Biosci. Biotechnol. Biochem., 59, 1012-1015 (1995).
3. Blackwood, A. D., and Bucke, C., Addition of polar organic solvents can improve the product selectivity of cyclodextrin glycosyltransferase solvent effects on CGTase. Enzyme Microb. Technol., 27, 704-708 (2000).
4. Lee, Y. D., and Kim, H. S., Enhancement of enzymatic production of cyclodextrins by organic solvents. Enzyme Microb. Technol., 13, 499-503 (1991).
5. G-a-D-glucopyranosyl-rutin. Agric. Biol. Chem., 55, 181-187 (1991).
6. Antonini, E., Carrea, G., and Cremonesi, P., Enzyme catalyzed reactions in water-organic solvent two-phase systems. Enzyme Microb. Technol., 3, 291-296 (1981).
7. Carrea, G., Biocatalysis in water-organic solvent two phase systems. Trends Biotechnol., 2, 102-106 (1984).
8. Ogino, H., Miyamoto, K., and Ishikawa, H., Organic-solvent-tolerant bacterium which secretes organic-solvent-stable lipolytic enzyme. Appl. Environ. Microbiol., 58, 145-146 (1994).
9. Doukyu, N., and Aono, R., Purification of extracellular cholesterol oxidase with high activity in the presence of organic solvents from Pseudomonas sp. strain ST-200. Appl. Environ. Microbiol., 64, 1929-1932 (1998).
10. Doukyu, N., and Aono, R., Cloning, sequence analysis and expression of a gene encoding an organic solvent- and detergent-tolerant cholesterol oxidase of Burkholderia cepacia strain ST-200. Appl. Microbiol. Biotechnol., 57, 146-152 (2001).
11. Miller, G. L., Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem., 31, 426-428 (1959).
12. Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
13. Laemmli, U. K., Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature, 224, 680-685 (1970).
14. Lane, D. J., Pace, B., Olsen, G. J., Stahl, D. A., Sogin, M. L., and Pace, N. R., Rapid determination of 16S ribosomal RNA sequences for phylogenetic analysis. Proc. Natl. Acad. Sci. USA, 82, 6955-6959 (1985).
15. Shida, O., Takagi, H., Kadowaki, K., Nakamura, L. K., and Komagata, K., Emended description of Paenibacillus amylolyticus and description of Paenibacillus illinoisensis sp. nov. and Paenibacillus chibensis sp. nov. Int. J. Sys. Bacteriol., 47, 299-306 (1997).
16. Tonkova, A., Bacterial cyclodextrin glucanotran-sferase. Enzyme Microb. Technol., 22, 678-686 (1998).
17. Laane, C., Boeren, S., Vos, K., and Veegar, C., Rules for optimization of biocatalysis in organic solvents. Biotechnol. Bioeng., 30, 81-87 (1987)